In the biopharmaceutical industry, the expression of complex recombinant protein drugs in mammalian cells (MC) has obvious advantages. MC can complete suitable post translation modification to ensure that the expressed recombinant proteins have formed proper disulfide bonds, glycosylation pattern and other complex protein structure to guarantee the safety and efficacy of these protein drugs. MC therefore is an important kind of expression system.
In recent years, animal cell culture technology for producing monoclonal antibodies in large-scale has been advanced rapidly. Technical progress in the field is mainly concentrated in the personalized media development and the process condition optimization, etc. Recombinant antibodies as one kind of biological macromolecules may have various forms due to aggregation, degradation, glycosylation modification, oxidation, acetoxylation, isomerization, and mismatched disulfide bonds. Purity of antibody is a decisive factor on the safety and efficacy of antibody molecules. Existing methods for improving antibody purity are mainly focusing on shortening the growth duration time of cell culture or modifying downstream purification methodology to increase purity but sacrifice yield. Decreasing cell culture duration time will reduce the final harvested antibody amount, and may also affect glycosylation pattern. Modifying downstream purification methodology may increase purity but sacrifice yield. As a result, novel cell culture approaches to significantly improve the antibody purity without reducing the final antibody product yield are needed.